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  • Articles  (48)
  • Computer Science  (48)
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  • Articles  (48)
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  • 1
    Publication Date: 2014-03-19
    Description: :  The ability to integrate and visualize experimental proteomic evidence in the context of rich protein feature annotations represents an unmet need of the proteomics community. Here we present Protter, a web-based tool that supports interactive protein data analysis and hypothesis generation by visualizing both annotated sequence features and experimental proteomic data in the context of protein topology. Protter supports numerous proteomic file formats and automatically integrates a variety of reference protein annotation sources, which can be readily extended via modular plug-ins. A built-in export function produces publication-quality customized protein illustrations, also for large datasets. Visualizations of surfaceome datasets show the specific utility of Protter for the integrated visual analysis of membrane proteins and peptide selection for targeted proteomics. Availability and implementation:  The Protter web application is available at http://wlab.ethz.ch/protter . Source code and installation instructions are available at http://ulo.github.io/Protter/ . Contact:   wbernd@ethz.ch Supplementary Information: Supplementary data are available at Bioinformatics online.
    Print ISSN: 1367-4803
    Electronic ISSN: 1460-2059
    Topics: Biology , Computer Science , Medicine
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  • 2
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2010-08-14
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roeb, Martin -- Muller-Steinhagen, Hans -- New York, N.Y. -- Science. 2010 Aug 13;329(5993):773-4. doi: 10.1126/science.1191137.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Technical Thermodynamics, Deutsches Zentrum fur Luft-und Raumfahrt, Linder Hoehe, Koeln, 51147 Germany. Martin.Roeb@dlr.de〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20705841" target="_blank"〉PubMed〈/a〉
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
    Publication Date: 2013-01-12
    Description: Historically, time measurements have been based on oscillation frequencies in systems of particles, from the motion of celestial bodies to atomic transitions. Relativity and quantum mechanics show that even a single particle of mass m determines a Compton frequency omega(0) = mc(2)/[formula: see text] where c is the speed of light and [formula: see text] is Planck's constant h divided by 2pi. A clock referenced to omega(0) would enable high-precision mass measurements and a fundamental definition of the second. We demonstrate such a clock using an optical frequency comb to self-reference a Ramsey-Borde atom interferometer and synchronize an oscillator at a subharmonic of omega(0.) This directly demonstrates the connection between time and mass. It allows measurement of microscopic masses with 4 x 10(-9) accuracy in the proposed revision to SI units. Together with the Avogadro project, it yields calibrated kilograms.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lan, Shau-Yu -- Kuan, Pei-Chen -- Estey, Brian -- English, Damon -- Brown, Justin M -- Hohensee, Michael A -- Muller, Holger -- New York, N.Y. -- Science. 2013 Feb 1;339(6119):554-7. doi: 10.1126/science.1230767. Epub 2013 Jan 10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physics, University of California-Berkeley, CA 94720, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23306441" target="_blank"〉PubMed〈/a〉
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
    Publication Date: 2006-10-28
    Description: The spindle assembly checkpoint guards the fidelity of chromosome segregation. It requires the close cooperation of cell cycle regulatory proteins and cytoskeletal elements to sense spindle integrity. The role of the centrosome, the organizing center of the microtubule cytoskeleton, in the spindle checkpoint is unclear. We found that the molecular requirements for a functional spindle checkpoint included components of the large gamma-tubulin ring complex (gamma-TuRC). However, their localization at the centrosome and centrosome integrity were not essential for this function. Thus, the spindle checkpoint can be activated at the level of microtubule nucleation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Muller, Hannah -- Fogeron, Marie-Laure -- Lehmann, Verena -- Lehrach, Hans -- Lange, Bodo M H -- New York, N.Y. -- Science. 2006 Oct 27;314(5799):654-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Vertebrate Genomics, Max-Planck Institute for Molecular Genetics, Ihnestrasse 73, D-14195 Berlin, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17068266" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Cycle Proteins/metabolism ; Cell Line ; Centrosome/physiology ; Drosophila Proteins/genetics/*metabolism ; Drosophila melanogaster ; Homeodomain Proteins/genetics/metabolism ; Humans ; Kinetochores/metabolism ; Microtubule-Associated Proteins/genetics/*metabolism ; Microtubules/ultrastructure ; *Mitosis ; Protein Kinases/metabolism ; Protein-Serine-Threonine Kinases ; RNA Interference ; Spindle Apparatus/*metabolism/ultrastructure ; Tubulin/*metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
    Publication Date: 2014-05-17
    Description: Nuclear magnetic resonance (NMR) spectroscopy is useful to determine molecular structure in tissues grown in vitro only if their fidelity, relative to native tissue, can be established. Here, we use multidimensional NMR spectra of animal and in vitro model tissues as fingerprints of their respective molecular structures, allowing us to compare the intact tissues at atomic length scales. To obtain spectra from animal tissues, we developed a heavy mouse enriched by about 20% in the NMR-active isotopes carbon-13 and nitrogen-15. The resulting spectra allowed us to refine an in vitro model of developing bone and to probe its detailed structure. The identification of an unexpected molecule, poly(adenosine diphosphate ribose), that may be implicated in calcification of the bone matrix, illustrates the analytical power of this approach.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chow, W Ying -- Rajan, Rakesh -- Muller, Karin H -- Reid, David G -- Skepper, Jeremy N -- Wong, Wai Ching -- Brooks, Roger A -- Green, Maggie -- Bihan, Dominique -- Farndale, Richard W -- Slatter, David A -- Shanahan, Catherine M -- Duer, Melinda J -- BB/G021392/1/Biotechnology and Biological Sciences Research Council/United Kingdom -- G0500707/Medical Research Council/United Kingdom -- PG/08/011/24416/British Heart Foundation/United Kingdom -- PG/10/43/28390/British Heart Foundation/United Kingdom -- RG/09/003/27122/British Heart Foundation/United Kingdom -- RG/11/14/29056/British Heart Foundation/United Kingdom -- New York, N.Y. -- Science. 2014 May 16;344(6185):742-6. doi: 10.1126/science.1248167.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK. ; Orthopaedic Research Unit, University of Cambridge, Addenbrooke's Hospital, Cambridge CB2 0QQ, UK. ; Department of Physiology, Development, and Neuroscience, University of Cambridge, Downing Site, Cambridge CB2 3DY, UK. ; Central Biomedical Resources, University of Cambridge, School of Clinical Medicine, West Forvie Building, Forvie Site, Robinson Way, Cambridge CB2 0SZ, UK. ; Department of Biochemistry, University of Cambridge, Downing Site, Cambridge CB2 1QW, UK. ; British Heart Foundation Centre of Research Excellence, Cardiovascular Division, James Black Centre, King's College London, 125 Coldharbour Lane, London SE5 9NU, UK. ; Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK. mjd13@cam.ac.uk.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/24833391" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Bone Development ; *Calcification, Physiologic ; Carbon Isotopes ; Extracellular Matrix/chemistry ; Growth Plate/growth & development ; Mice ; Models, Biological ; Nitrogen Isotopes ; Nuclear Magnetic Resonance, Biomolecular/*methods ; Poly Adenosine Diphosphate Ribose/*analysis ; Sheep
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 6
    Publication Date: 2014-03-29
    Description: Rapid advances in DNA synthesis techniques have made it possible to engineer viruses, biochemical pathways and assemble bacterial genomes. Here, we report the synthesis of a functional 272,871-base pair designer eukaryotic chromosome, synIII, which is based on the 316,617-base pair native Saccharomyces cerevisiae chromosome III. Changes to synIII include TAG/TAA stop-codon replacements, deletion of subtelomeric regions, introns, transfer RNAs, transposons, and silent mating loci as well as insertion of loxPsym sites to enable genome scrambling. SynIII is functional in S. cerevisiae. Scrambling of the chromosome in a heterozygous diploid reveals a large increase in a-mater derivatives resulting from loss of the MATalpha allele on synIII. The complete design and synthesis of synIII establishes S. cerevisiae as the basis for designer eukaryotic genome biology.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4033833/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4033833/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Annaluru, Narayana -- Muller, Heloise -- Mitchell, Leslie A -- Ramalingam, Sivaprakash -- Stracquadanio, Giovanni -- Richardson, Sarah M -- Dymond, Jessica S -- Kuang, Zheng -- Scheifele, Lisa Z -- Cooper, Eric M -- Cai, Yizhi -- Zeller, Karen -- Agmon, Neta -- Han, Jeffrey S -- Hadjithomas, Michalis -- Tullman, Jennifer -- Caravelli, Katrina -- Cirelli, Kimberly -- Guo, Zheyuan -- London, Viktoriya -- Yeluru, Apurva -- Murugan, Sindurathy -- Kandavelou, Karthikeyan -- Agier, Nicolas -- Fischer, Gilles -- Yang, Kun -- Martin, J Andrew -- Bilgel, Murat -- Bohutski, Pavlo -- Boulier, Kristin M -- Capaldo, Brian J -- Chang, Joy -- Charoen, Kristie -- Choi, Woo Jin -- Deng, Peter -- DiCarlo, James E -- Doong, Judy -- Dunn, Jessilyn -- Feinberg, Jason I -- Fernandez, Christopher -- Floria, Charlotte E -- Gladowski, David -- Hadidi, Pasha -- Ishizuka, Isabel -- Jabbari, Javaneh -- Lau, Calvin Y L -- Lee, Pablo A -- Li, Sean -- Lin, Denise -- Linder, Matthias E -- Ling, Jonathan -- Liu, Jaime -- Liu, Jonathan -- London, Mariya -- Ma, Henry -- Mao, Jessica -- McDade, Jessica E -- McMillan, Alexandra -- Moore, Aaron M -- Oh, Won Chan -- Ouyang, Yu -- Patel, Ruchi -- Paul, Marina -- Paulsen, Laura C -- Qiu, Judy -- Rhee, Alex -- Rubashkin, Matthew G -- Soh, Ina Y -- Sotuyo, Nathaniel E -- Srinivas, Venkatesh -- Suarez, Allison -- Wong, Andy -- Wong, Remus -- Xie, Wei Rose -- Xu, Yijie -- Yu, Allen T -- Koszul, Romain -- Bader, Joel S -- Boeke, Jef D -- Chandrasegaran, Srinivasan -- 092076/Wellcome Trust/United Kingdom -- GM077291/GM/NIGMS NIH HHS/ -- R01 GM077291/GM/NIGMS NIH HHS/ -- R01 GM090192/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2014 Apr 4;344(6179):55-8. doi: 10.1126/science.1249252. Epub 2014 Mar 27.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Environmental Health Sciences, Johns Hopkins University (JHU) School of Public Health, Baltimore, MD 21205, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/24674868" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; *Chromosomes, Fungal/genetics/metabolism ; DNA, Fungal/genetics ; Genes, Fungal ; Genetic Fitness ; Genome, Fungal ; Genomic Instability ; Introns ; Molecular Sequence Data ; Mutation ; Polymerase Chain Reaction ; RNA, Fungal/genetics ; RNA, Transfer/genetics ; Saccharomyces cerevisiae/cytology/*genetics/physiology ; Sequence Analysis, DNA ; Sequence Deletion ; Synthetic Biology/*methods ; Transformation, Genetic
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 7
    Publication Date: 2015-08-22
    Description: If dark energy, which drives the accelerated expansion of the universe, consists of a light scalar field, it might be detectable as a "fifth force" between normal-matter objects, in potential conflict with precision tests of gravity. Chameleon fields and other theories with screening mechanisms, however, can evade these tests by suppressing the forces in regions of high density, such as the laboratory. Using a cesium matter-wave interferometer near a spherical mass in an ultrahigh-vacuum chamber, we reduced the screening mechanism by probing the field with individual atoms rather than with bulk matter. We thereby constrained a wide class of dark energy theories, including a range of chameleon and other theories that reproduce the observed cosmic acceleration.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hamilton, P -- Jaffe, M -- Haslinger, P -- Simmons, Q -- Muller, H -- Khoury, J -- New York, N.Y. -- Science. 2015 Aug 21;349(6250):849-51. doi: 10.1126/science.aaa8883.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physics, 366 Le Conte Hall MS 7300, University of California-Berkeley, Berkeley, CA 94720, USA. ; Department of Physics, 366 Le Conte Hall MS 7300, University of California-Berkeley, Berkeley, CA 94720, USA. Lawrence Berkeley National Laboratory, One Cyclotron Road, Berkeley, CA 94720, USA. hm@berkeley.edu. ; Center for Particle Cosmology, Department of Physics and Astronomy, University of Pennsylvania, Philadelphia, PA 19104, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/26293958" target="_blank"〉PubMed〈/a〉
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 8
    Publication Date: 2016-04-30
    Description: The cytochrome bd oxidases are terminal oxidases that are present in bacteria and archaea. They reduce molecular oxygen (dioxygen) to water, avoiding the production of reactive oxygen species. In addition to their contribution to the proton motive force, they mediate viability under oxygen-related stress conditions and confer tolerance to nitric oxide, thus contributing to the virulence of pathogenic bacteria. Here we present the atomic structure of the bd oxidase from Geobacillus thermodenitrificans, revealing a pseudosymmetrical subunit fold. The arrangement and order of the heme cofactors support the conclusions from spectroscopic measurements that the cleavage of the dioxygen bond may be mechanistically similar to that in the heme-copper-containing oxidases, even though the structures are completely different.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Safarian, Schara -- Rajendran, Chitra -- Muller, Hannelore -- Preu, Julia -- Langer, Julian D -- Ovchinnikov, Sergey -- Hirose, Taichiro -- Kusumoto, Tomoichirou -- Sakamoto, Junshi -- Michel, Hartmut -- R01GM092802/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2016 Apr 29;352(6285):583-6. doi: 10.1126/science.aaf2477.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max-von-Laue-Strasse 3, D-60438 Frankfurt/Main, Germany. ; Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max-von-Laue-Strasse 3, D-60438 Frankfurt/Main, Germany. Present address: Faculty of Biology and Preclinical Medicine, University of Regensburg, Universitatsstrasse 31, D-93051 Regensburg, Germany. ; Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max-von-Laue-Strasse 3, D-60438 Frankfurt/Main, Germany. Present address: Department of Molecular Membrane Biology, Max Planck Institute for Brain Research, Max-von-Laue-Strasse 4, D-60438 Frankfurt/Main, Germany. ; Department of Biochemistry, University of Washington, Seattle, WA, USA. ; Department of Bioscience and Bioinformatics, Kyushu Institute of Technology, Kawazu 680-4, Iizuka, Fukuoka-ken 820-8502, Japan. ; Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max-von-Laue-Strasse 3, D-60438 Frankfurt/Main, Germany. hartmut.michel@biophys.mpg.de.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/27126043" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins/*chemistry/ultrastructure ; Cytochrome d Group/*chemistry/ultrastructure ; Cytochromes b/*chemistry/ultrastructure ; Electron Transport Complex IV/*chemistry/ultrastructure ; Geobacillus/*enzymology ; Oxygen/*chemistry ; Protein Folding ; Protein Structure, Secondary
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 9
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1984-06-08
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Muller, E H -- New York, N.Y. -- Science. 1984 Jun 8;224(4653):1091-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17735244" target="_blank"〉PubMed〈/a〉
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 10
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1981-09-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Muller-Beck, H -- New York, N.Y. -- Science. 1981 Sep 11;213(4513):1241-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17744753" target="_blank"〉PubMed〈/a〉
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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